Evolution of the vertebrate glucose-dependent insulinotropic polypeptide (GIP) gene

Irwin, David M.; Zhang, Tony

doi:10.1016/j.cbd.2006.09.001

Cited by 19 publications

(22 citation statements)

References 42 publications

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“…These observations represent the first instance in which GIP expression has been localized to the pancreas and the initial demonstration of GIP and insulin coexpression. Previous studies conducted in our laboratory and by others (14) have shown that of the five fully sequenced members of the Actinopterygii class (zebrafish, medaka, fugu, tetraodon, and stickleback), the zebrafish is the only species to possess a GIP-like sequence. This expression pattern suggests that the Actinopterygii might be the first evolutionary lineage in which a GIP-like protein exists and supports the theory that the enteroinsular axis may have evolved in the zebrafish by virtue of being the earliest vertebrate identified to express GIP (14).…”

Section: Discussionmentioning

confidence: 70%

Expression of glucose-dependent insulinotropic polypeptide in the zebrafish

Musson

Jepeal

Mabray³

et al. 2009

American Journal of Physiology-Regulatory, Integrative and Comp

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In mammals, glucose-dependent insulinotropic polypeptide (GIP) is synthesized predominately in the small intestine and functions in conjunction with insulin to promote nutrient deposition. However, little is known regarding GIP expression and function in early vertebrates like the zebrafish, a model organism representing an early stage in the evolutionary development of the compound vertebrate pancreas. Analysis of GIP and insulin (insa) expression in zebrafish larvae by RT-PCR demonstrated that although insa was detected as early as 24 h postfertilization (hpf), GIP expression was not demonstrated until 72 hpf, shortly after the completion of endocrine pancreatic development but prior to the commencement of independent feeding. Furthermore, whole mount in situ hybridization of zebrafish larvae showed expression of GIP and insa in the same tissues, and in adult zebrafish, RT-PCR and immunohistochemistry demonstrated GIP expression in both the intestine and the pancreas. Receptor activation studies showed that zebrafish GIP was capable of activating the rat GIP receptor. Although previous studies have identified four receptors with glucagon receptor-like sequences in the zebrafish, one of which possesses the capacity to bind GIP, a functional analysis of these receptors has not been performed. This study demonstrates interactions between the latter receptor and zebrafish GIP, identifying it as a potential in vivo target for the ligand. Finally, food deprivation studies in larvae demonstrated an increase in GIP and proglucagon II mRNA levels in response to fasting. In conclusion, the results of these studies suggest that although the zebrafish appears to be a model of an early stage of evolutionary development of GIP expression, the peptide may not possess incretin properties in this species.

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Section: Discussionmentioning

confidence: 70%

Expression of glucose-dependent insulinotropic polypeptide in the zebrafish

Musson

Jepeal

Mabray³

et al. 2009

American Journal of Physiology-Regulatory, Integrative and Comp

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“…For glucagon, this has occurred in the Osteichthyes lineage and another in hystricomorphic rodents whose glucagons are known to have had a change in biological activity 13–15 . For GIP, an episode between fish and tetrapods has resulted in lengthening of the peptide whereas another in early mammals has lead to change in function 15,16 . The shorter 31 amino acids length of fish GIP may therefore have greater resemblance to the ancestral form 15 (Table 1).…”

Section: Phylogeny Of Proglucagon‐derived Peptidesmentioning

confidence: 99%

Insights into the evolution of proglucagon‐derived peptides and receptors in fish and amphibians

Ng¹,

Lee²,

Chow³

2010

Annals of the New York Academy of Sciences

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Glucagon and the glucagon-like peptides (GLP-1 and GLP-2) share a common evolutionary origin and are triplication products of an ancestral glucagon exon. In mammals, a standard scenario is found where only a single proglucagon-derived peptide set exists. However, fish and amphibians have either multiple proglucagon genes or exons that are likely resultant of duplication events. Through phylogenetic analysis and examination of their respective functions, the proglucagon ligand-receptor pairs are believed to have evolved independently before acquiring specificity for one another. This review will provide a comprehensive overview of current knowledge of proglucagon-derived peptides and receptors, with particular focus on fish and amphibian species.

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“…Interestingly however, an analysis of the GIP gene in different vertebrates suggests that certain species such as the zebrafish (Danio rerio) produces GIP instead of GIP (13). Although GIP is not currently recognized as a natural form of GIP in mammals, mammalian pro-GIP contains a highly conserved PC2 cleavage site (KGKK) at residues 52-55 (13). A recent analysis of the GIP fragments following coinfection of GH4 cells with adenoviral vectors expressing pro-GIP and PC2 confirmed that GIP could be produced (39).…”

mentioning

confidence: 99%

Differential processing of pro-glucose-dependent insulinotropic polypeptide in gut

Fujita

Asadi

Yang

et al. 2010

American Journal of Physiology-Gastrointestinal and Liver Physi

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Glucose-dependent insulinotropic polypeptide (GIP) is a hormone released from enteroendocrine K cells in response to meals. Posttranslational processing of the precursor protein pro-GIP at residue 65 by proprotein convertase subtilisin/kexin type 1 (PC1/3) in gut K cells gives rise to the established 42-amino-acid form of GIP (GIP1–42). However, the pro-GIP peptide sequence contains a consensus cleavage site for PC2 at residues 52–55 and we identified PC2 immunoreactivity in a subset of K cells, suggesting the potential existence of a COOH-terminal truncated GIP isoform, GIP1–30. Indeed a subset of mouse and human K cells display GIP immunoreactivity with GIP antibodies directed to the mid portion of the peptide, but not with a COOH-terminal-directed GIP antibody, indicative of the presence of a truncated form of GIP. This population of cells represents ∼5–15% of the total GIP-immunoreactive cells in mice, depending on the region of intestine, and is virtually absent in mice lacking PC2. Amidated GIP1–30 and GIP1–42 have comparable potency at stimulating somatostatin release in the perfused mouse stomach. Therefore, GIP1–30 represents a naturally occurring, biologically active form of GIP.

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Evolution of the vertebrate glucose-dependent insulinotropic polypeptide (GIP) gene

Cited by 19 publications

References 42 publications

Expression of glucose-dependent insulinotropic polypeptide in the zebrafish

Expression of glucose-dependent insulinotropic polypeptide in the zebrafish

Insights into the evolution of proglucagon‐derived peptides and receptors in fish and amphibians

Differential processing of pro-glucose-dependent insulinotropic polypeptide in gut

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